Search Results

Overview

Uniprot IDP18669
Protein NamePhosphoglycerate mutase 1
Gene NamePGAM1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
100 GGLTGLNKAETAAKH
106 NKAETAAKHGEAQVK
113 KHGEAQVKIWRRSYD
138 PFYSNISKDRRYADL
157 LPSCESLKDTIARAL
241 GDEETVRKAMEAVAA
251 EAVAAQGKAKK****
253 VAAQGKAKK******
39 PAGHEEAKRGGQALR

Function

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate, a crucial step in glycolysis, by using 2,3-bisphosphoglycerate (PubMed:23653202). Also catalyzes the interconversion of (2R)-2,3-bisphosphoglycerate and (2R)-3-phospho-glyceroyl phosphate (PubMed:23653202)

Protein Sequence

10 MAAYKLVLIR 20 HGESAWNLEN 30 RFSGWYDADL 40 SPAGHEEAKR 50 GGQALRDAGY 60 EFDICFTSVQ 70 KRAIRTLWTV 80 LDAIDQMWLP 90 VVRTWRLNER 100 HYGGLTGLNK 110 AETAAKHGEA 120 QVKIWRRSYD 130 VPPPPMEPDH 140 PFYSNISKDR 150 RYADLTEDQL 160 PSCESLKDTI 170 ARALPFWNEE 180 IVPQIKEGKR 190 VLIAAHGNSL 200 RGIVKHLEGL 210 SEEAIMELNL 220 PTGIPIVYEL 230 DKNLKPIKPM 240 QFLGDEETVR 250 KAMEAVAAQG KAKK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:1904813 ficolin-1-rich granule lumen
Cellular Component GO:0016020 membrane
Cellular Component GO:0034774 secretory granule lumen
Molecular Function GO:0004082 bisphosphoglycerate mutase activity
Molecular Function GO:0016787 hydrolase activity
Molecular Function GO:0004619 phosphoglycerate mutase activity
Molecular Function GO:0019901 protein kinase binding
Biological Process GO:0061621 canonical glycolysis
Biological Process GO:0006094 gluconeogenesis

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[4] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[5] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[6] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[7] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[8] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[9] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.